scholarly journals Novel Natural Angiotensin Converting Enzyme (ACE)-Inhibitory Peptides Derived from Sea Cucumber-Modified Hydrolysates by Adding Exogenous Proline and a Study of Their Structure–Activity Relationship

Marine Drugs ◽  
2018 ◽  
Vol 16 (8) ◽  
pp. 271 ◽  
Author(s):  
Jianpeng Li ◽  
Zunying Liu ◽  
Yuanhui Zhao ◽  
Xiaojie Zhu ◽  
Rilei Yu ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Sea Cucumber ◽  
Antihypertensive Drugs ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory ◽  
Exogenous Proline

Natural angiotensin converting enzyme (ACE)-inhibitory peptides, which are derived from marine products, are useful as antihypertensive drugs. Nevertheless, the activities of these natural peptides are relatively low, which limits their applications. The aim of this study was to prepare efficient ACE-inhibitory peptides from sea cucumber-modified hydrolysates by adding exogenous proline according to a facile plastein reaction. When 40% proline (w/w, proline/free amino groups) was added, the modified hydrolysates exhibited higher ACE-inhibitory activity than the original hydrolysates. Among the modified hydrolysates, two novel efficient ACE-inhibitory peptides, which are namely PNVA and PNLG, were purified and identified by a sequential approach combining a sephadex G-15 gel column, reverse-phase high-performance liquid chromatography (RP-HPLC) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS), before we conducted confirmatory studies with synthetic peptides. The ACE-inhibitory activity assay showed that PNVA and PNLG exhibited lower IC50 values of 8.18 ± 0.24 and 13.16 ± 0.39 μM than their corresponding truncated analogs (NVA and NLG), respectively. Molecular docking showed that PNVA and PNLG formed a larger number of hydrogen bonds with ACE than NVA and NLG, while the proline at the N-terminal of peptides can affect the orientation of the binding site of ACE. The method developed in this study may potentially be applied to prepare efficient ACE-inhibitory peptides, which may play a key role in hypertension management.

Insects as source of angiotensin converting enzyme inhibitory peptides

2017 ◽  
Vol 3 (4) ◽  
pp. 231-240 ◽  
Author(s):  
A. Cito ◽  
M. Botta ◽  
V. Francardi ◽  
E. Dreassi
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Hypertension Treatment ◽  
Converting Enzyme ◽  
Oecophylla Smaragdina ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Hypertension is well known as one of the major risk for cardiovascular diseases which annually affect millions of people. The angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation process. Indeed, hypertension treatment by synthetic ACE inhibitors (e.g. captopril, lisinopril and ramipril) is effective; however, their use can cause serious side effects, such as hypotension, cough, reduced renal function and angioedema. Thus, research was focused on natural ACE inhibitory peptides sources such as foodstuffs and also, more recently, edible insects. In the last decades, ACE inhibitory activity has been detected in protein hydrolysates from insect species belonging to the orders of Coleoptera, Diptera, Hymenoptera, Lepidoptera and also Orthoptera. Further investigations led to identify specific ACE inhibitory peptides from the silkworm Bombyx mori (Lepidoptera: Bombycidae), the yellow mealworm Tenebrio molitor (Coleoptera: Tenebrionidae), the cotton leafworm Spodoptera littoralis (Lepidoptera: Noctuidae) and also from the weaver ant Oecophylla smaragdina (Hymenoptera: Formicidae). Even if ACE inhibitory activity of these bioactive peptides has been in vitro assayed and is comparable to those of some bioactive peptides derived from other animal protein sources, the in vivo effectiveness of most of these bioactive peptides still needs to be confirmed. The aim of this review is to present an outline of the currently available data on the potential use of insects for hypertension treatment with a focus on the ACE inhibitory peptides identified in these invertebrates to date.

scholarly journals Angiotensin I-Converting-Enzyme-Inhibitory and Antibacterial Peptides from Lactobacillus helveticus PR4 Proteinase-Hydrolyzed Caseins of Milk from Six Species

2003 ◽  
Vol 69 (9) ◽  
pp. 5297-5305 ◽  
Author(s):  
F. Minervini ◽  
F. Algaron ◽  
C. G. Rizzello ◽  
P. F. Fox ◽  
V. Monnet ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Sodium Caseinate ◽  
Lactobacillus Helveticus ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

ABSTRACT Sodium caseinates prepared from bovine, sheep, goat, pig, buffalo or human milk were hydrolyzed by a partially purified proteinase of Lactobacillus helveticus PR4. Peptides in each hydrolysate were fractionated by reversed-phase fast-protein liquid chromatography. The fractions which showed the highest angiotensin I-converting-enzyme (ACE)-inhibitory or antibacterial activity were sequenced by mass spectrum and Edman degradation analyses. Various ACE-inhibitory peptides were found in the hydrolysates: the bovine αS1-casein (αS1-CN) 24-47 fragment (f24-47), f169-193, and β-CN f58-76; ovine αS1-CN f1-6 and αS2-CN f182-185 and f186-188; caprine β-CN f58-65 and αS2-CN f182-187; buffalo β-CN f58-66; and a mixture of three tripeptides originating from human β-CN. A mixture of peptides with a C-terminal sequence, Pro-Gly-Pro, was found in the most active fraction of the pig sodium caseinate hydrolysate. The highest ACE-inhibitory activity of some peptides corresponded to the concentration of the ACE inhibitor (S)-N-(1-[ethoxycarbonyl]-3-phenylpropyl)-ala-pro maleate (enalapril) of 49.253 μg/ml (100 μmol/liter). Several of the above sequences had features in common with other ACE-inhibitory peptides reported in the literature. The 50% inhibitory concentration (IC50) of some of the crude peptide fractions was very low (16 to 100 μg/ml). Some identified peptides were chemically synthesized, and the ACE-inhibitory activity and IC50s were confirmed. An antibacterial peptide corresponding to β-CN f184-210 was identified in human sodium caseinate hydrolysate. It showed a very large spectrum of inhibition against gram-positive and -negative bacteria, including species of potential clinical interest, such as Enterococcus faecium, Bacillus megaterium, Escherichia coli, Listeria innocua, Salmonella spp., Yersinia enterocolitica, and Staphylococcus aureus. The MIC for E. coli F19 was ca. 50 μg/ml. Once generated, the bioactive peptides were resistant to further degradation by proteinase of L. helveticus PR4 or by trypsin and chymotrypsin.

scholarly journals Angiotensin-converting enzyme (ACE) inhibitory activity of Solanum torvum and isolation of a novel methyl salicylate glycoside

2014 ◽  
Vol 11 ◽  
pp. 557-562 ◽  
Author(s):  
Arunee Simaratanamongkol ◽  
Kaoru Umehara ◽  
Hiroki Niki ◽  
Hiroshi Noguchi ◽  
Pharkphoom Panichayupakaranant
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Methyl Salicylate ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Solanum Torvum ◽  
Ace Inhibitory

scholarly journals Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 101 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Chunju Bao ◽  
Jiangpeng Meng ◽  
He Chen ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Goat Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human αs1-casein expressed in Escherichia coli

1999 ◽  
Vol 66 (3) ◽  
pp. 431-439 ◽  
Author(s):  
YOO-KYEONG KIM ◽  
SUN YOON ◽  
DAE-YEUL YU ◽  
BO LÖNNERDAL ◽  
BONG-HYUN CHUNG
Keyword(s):  
Escherichia Coli ◽  
Amino Acid Sequences ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Treatment Of Hypertension ◽  
Ace Inhibitory

Recombinant human αs1-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II, B-II and C, were isolated and their amino acid sequences identified as Tyr–Pro–Glu–Arg (residues 8–11), Tyr–Tyr–Pro–Gln–Ile–Met–Gln–Tyr (residues 136–143) and Asn–Asn–Val–Met–Leu–Gln–Trp (residues 164–170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132·5, 24·8 and 41·0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.

Insight into the binding of ACE-inhibitory peptides to angiotensin-converting enzyme: a molecular simulation

2018 ◽  
Vol 45 (3) ◽  
pp. 215-222 ◽  
Author(s):  
Zhenyan Jiang ◽  
Hansi Zhang ◽  
Xuefeng Bian ◽  
Jingfeng Li ◽  
Jing Li ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Molecular Simulation ◽  
Converting Enzyme ◽  
Inhibitory Peptides ◽  
Ace Inhibitory Peptides ◽  
Insight Into ◽  
Ace Inhibitory

scholarly journals The Potential Angiotensin-Converting Enzyme Inhibitory Activity of Oleanolic Acid in the Hydroethanolic Extract of Crataegus monogyna Jacq

2006 ◽  
Vol 1 (5) ◽  
pp. 1934578X0600100 ◽  
Author(s):  
Everaldo Attard ◽  
Henrietta Attard
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Oleanolic Acid ◽  
Inhibitory Activity ◽  
Acid Group ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Crataegus Monogyna ◽  
Triterpenic Acids ◽  
Hydroethanolic Extract ◽  
Ace Inhibitory

The hydroethanolic extract of Crataegus monogyna was studied for its chemical constitution and angiotensin-converting enzyme (ACE) inhibitory activity. The extract contained triterpenic acids, flavonoids and coumarins. The ACE inhibitory activity was studied using captropril, as a control drug, and oleanolic acid, as a constituent of the hydroethanolic extract and a member of the triterpenic acid group. The hydroethanolic extract and oleanolic acid showed higher IC50 values (335.00 μg/mL and 3.61 μM, respectively) in comparison to captopril (46.9 nM). However, these results indicate the anti-ACE activity of oleanolic acid and the triterpenic acids, which has not been demonstrated earlier for hawthorn extracts. In previous studies, the ACE inhibitory activity of C. monogyna extracts was always attributed to flavonoids and proanthocyanidins.

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